Evidence map›Paper›PMID 25717183›Full record

ArticleMolecular biology of the cell2015

Crucial role for the LSP1-myosin1e bimolecular complex in the regulation of Fcγ receptor-driven phagocytosis.

Sebastian Maxeiner, Nian Shi, Carmen Schalla, Guelcan Aydin, Mareike Hoss, Simon Vogel, Martin Zenke, Antonio S Sechi

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 36 citations in OpenAlex.

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  10. LSP1-myosin1e bimolecular complex regulates focal adhesion dynamics and cell migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Sebastian MaxeinerInstitute of Biomedical Engineering, Department of Cell Biology, Applied Ecology, D-52074 Aachen, Germany.
Nian ShiInstitute of Biomedical Engineering, Department of Cell Biology, Applied Ecology, D-52074 Aachen, Germany.
Carmen SchallaInstitute of Biomedical Engineering, Department of Cell Biology, Applied Ecology, D-52074 Aachen, Germany.
Guelcan AydinInstitute of Biomedical Engineering, Department of Cell Biology, Applied Ecology, D-52074 Aachen, Germany.
Mareike HossElectron Microscopy Facility, Uniklinik RWTH Aachen, Applied Ecology, D-52074 Aachen, Germany.
Simon VogelFraunhofer Institute for Molecular Biology and Applied Ecology, D-52074 Aachen, Germany.
Martin ZenkeInstitute of Biomedical Engineering, Department of Cell Biology, Applied Ecology, D-52074 Aachen, Germany.
Antonio S SechiInstitute of Biomedical Engineering, Department of Cell Biology, Applied Ecology, D-52074 Aachen, Germany antonio.sechi@rwth-aachen.de.
Fraunhofer Institute for Molecular Biology and Applied Ecology · DEUniversitätsklinikum Aachen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin cytoskeleton remodeling is fundamental for Fcγ receptor-driven phagocytosis. In this study, we find that the leukocyte-specific protein 1 (LSP1) localizes to nascent phagocytic cups during Fcγ receptor-mediated phagocytosis, where it displays the same spatial and temporal distribution as the actin cytoskeleton. Down-regulation of LSP1 severely reduces the phagocytic activity of macrophages, clearly demonstrating a crucial role for this protein in Fcγ receptor-mediated phagocytosis. We also find that LSP1 binds to the class I molecular motor myosin1e. LSP1 interacts with the SH3 domain of myosin1e, and the localization and dynamics of both proteins in nascent phagocytic cups mirror those of actin. Furthermore, inhibition of LSP1-myosin1e and LSP1-actin interactions profoundly impairs pseudopodial formation around opsonized targets and their subsequent internalization. Thus the LSP1-myosin1e bimolecular complex plays a pivotal role in the regulation of actin cytoskeleton remodeling during Fcγ receptor-driven phagocytosis.

Indexed as

PhagocytosisAnimalsCalcium-Binding ProteinsMiceMicrofilament ProteinsMyosinsMyosin Type INIH 3T3 CellsProtein TransportReceptors, IgGCalcium-Binding ProteinsLsp1 protein, mouseMicrofilament ProteinsMyo1e protein, mouseMyosinsMyosin Type IReceptors, IgG

Identifiers

PMID25717183
PMCPMC4436777
OpenAlexW2070392595

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.